Sequence analysis of lens beta-crystallins suggests involvement of calpain in cataract formation.
作者： L.L. David , T.R. Shearer , M. Shih
DOI: 10.1016/S0021-9258(18)53944-2
关键词: Peptide sequence 、 Enzyme 、 Biochemistry 、 Crystallin 、 Calpain 、 Amino acid 、 Biology 、 Protease 、 Cataracts 、 Lens protein
摘要: Abnormal activation of the protease calpain in lens may be a cause cataracts. Cataracts were induced 10-day-old rats by single overdose sodium selenite. The water-insoluble protein from opaque nucleus was separated two-dimensional electrophoresis, electroblotted onto membranes, and NH2-terminal sequence partially degraded beta-crystallin polypeptides determined. Selenite cataractous lenses contained four major structural proteins, beta B1, B3, A3/A1, A4 crystallins, missing 5 to 49 amino acids their NH2 termini. Incubation intact beta-crystallins with II vitro produced identical cleavage sites. This provided further evidence for role production light scattering insoluble also suggested that similar process lead insolubilization during aging.
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sci-hub.st 参考文章(17)
L L David, T R Shearer, Calcium-activated proteolysis in the lens nucleus during selenite cataractogenesis. Investigative Ophthalmology & Visual Science. ,vol. 25, pp. 1275- 1283 ,(1984)
L L David, T R Shearer, K R Hightower, Regional Distribution of Free Calcium in Selenite Cataract: Relation to Calpain II Investigative Ophthalmology & Visual Science. ,vol. 28, pp. 1702- 1706 ,(1987)
L L David, T R Shearer, B M Dickey, Origin of urea-soluble protein in the selenite cataract. Role of beta-crystallin proteolysis and calpain II. Investigative Ophthalmology & Visual Science. ,vol. 28, pp. 1148- 1156 ,(1987)
L L David, T R Shearer, T Murachi, M Azuma, Amelioration of cataracts and proteolysis in cultured lenses by cysteine protease inhibitor E64. Investigative Ophthalmology & Visual Science. ,vol. 32, pp. 533- 540 ,(1991)
R. Lapatto, V. Nalini, B. Bax, H. Driessen, P.F. Lindley, T.L. Blundell, C. Slingsby, High resolution structure of an oligomeric eye lens β-crystallin : loops, arches, linkers and interfaces in βB2 dimer compared to a monomeric γ-crystallin Journal of Molecular Biology. ,vol. 222, pp. 1067- 1083 ,(1991) , 10.1016/0022-2836(91)90594-V
P. Matsudaira, Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. Journal of Biological Chemistry. ,vol. 262, pp. 10035- 10038 ,(1987) , 10.1016/S0021-9258(18)61070-1
Peter Johnson, Calpains (intracellular calcium-activated cysteine proteinases): structure-activity relationships and involvement in normal and abnormal cellular metabolism. International Journal of Biochemistry. ,vol. 22, pp. 811- 822 ,(1990) , 10.1016/0020-711X(90)90284-A
Mitsuyoshi Azuma, Thomas R. Shearer, Involvement of calpain in diamide-induced cataract in cultured lenses. FEBS Letters. ,vol. 307, pp. 313- 317 ,(1992) , 10.1016/0014-5793(92)80703-J
Mitsuyoshi Azuma, Larry L. David, Thomas R. Shearer, Hydration and elevated calcium alone do not produce xylose nuclear cataract: role of proteolysis by calpain. Ophthalmic Research. ,vol. 24, pp. 8- 14 ,(1992) , 10.1159/000267138
Charlotte A. Peterson, Joram Piatigorsky, Preferential conservation of the globular domains of the βA3/A1-crystallin polypeptide of the chicken eye lens Gene. ,vol. 45, pp. 139- 147 ,(1986) , 10.1016/0378-1119(86)90248-9